Effect of an Asymmetrically Arranged Equatorial Chelate Ring in an Active Site of Nitrile Hydratase

2008 ◽  
Vol 37 (1) ◽  
pp. 66-67 ◽  
Author(s):  
Takuma Yano ◽  
Yuko Wasada-Tsutsui ◽  
Yuji Kajita ◽  
Tomonori Shibayama ◽  
Yasuhiro Funahasi ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Chelate Ring

scholarly journals Identification of an Active Site-bound Nitrile Hydratase Intermediate through Single Turnover Stopped-flow Spectroscopy

2013 ◽  
Vol 288 (22) ◽  
pp. 15532-15536 ◽  
Author(s):  
Natalie Gumataotao ◽  
Misty L. Kuhn ◽  
Natalia Hajnas ◽  
Richard C. Holz
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Stopped Flow ◽  
Single Turnover

Role of the Amide Carbonyl Groups in the Nitrile Hydratase Active Site for Nitrile Coordination Using Co(III) Complex with N2S3-type Ligand

2015 ◽  
Vol 44 (6) ◽  
pp. 761-763 ◽  
Author(s):  
Takuma Yano ◽  
Tomohiro Ikeda ◽  
Tomonori Shibayama ◽  
Tomohiko Inomata ◽  
Yasuhiro Funahashi ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Carbonyl Groups ◽  
Amide Carbonyl

Iron complexes with an N/S chromophore relevant to the active site of the hydrolytic metalloenzyme nitrile hydratase

1997 ◽  
pp. 1711-1712 ◽  
Author(s):  
Alexandre L. Nivorozhkin ◽  
Ali I. Uraev ◽  
Gennadii I. Bondarenko ◽  
Alla S. Antsyshkina ◽  
Vasilii P. Kurbatov ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Iron Complexes ◽  
Hydrolytic Metalloenzyme

scholarly journals Analyzing the catalytic role of active site residues in the Fe-type nitrile hydratase from Comamonas testosteroni Ni1

2015 ◽  
Vol 20 (5) ◽  
pp. 885-894 ◽  
Author(s):  
Salette Martinez ◽  
Rui Wu ◽  
Karoline Krzywda ◽  
Veronika Opalka ◽  
Hei Chan ◽  
...  
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Comamonas Testosteroni ◽  
Active Site Residues ◽  
Catalytic Role

scholarly journals Insight into the Maturation Process of the Nitrile Hydratase Active Site

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Irene Ogutu ◽  
Richard Holz ◽  
Brian Bennett
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Maturation Process ◽  
Insight Into

scholarly journals Evidence for a dynamic role for homocitrate during nitrogen fixation: the effect of substitution at the α-Lys426 position in MoFe-protein of Azotobacter vinelandii

2006 ◽  
Vol 397 (2) ◽  
pp. 261-270 ◽  
Author(s):  
Marcus C. Durrant ◽  
Amanda Francis ◽  
David J. Lowe ◽  
William E. Newton ◽  
Karl Fisher
Keyword(s):  
Active Site ◽  
Ring Opening ◽  
Azotobacter Vinelandii ◽  
Chelate Ring ◽  
Wild Type ◽  
Biologically Relevant ◽  
Mofe Protein ◽  
Key Players ◽  
Femo Cofactor ◽  
The Subject

Although it is generally accepted that the active site of nitrogenase is located on the FeMo-cofactor, the exact site(s) of N2 binding and reduction remain the subject of continuing debate, with both molybdenum and iron atoms being suggested as key players. The current consensus favours binding of acetylene and some other non-biologically relevant substrates to the central iron atoms of the FeMo-cofactor [Dos Santos, Igarashi, Lee, Hoffman, Seefeldt and Dean (2005) Acc. Chem. Res. 38, 208–214]. The reduction of N2 is, however, a more demanding process than reduction of these alternative substrates because it has a much higher activation energy and does not bind until three electrons have been accumulated on the enzyme. The possible conversion of bidentate into monodentate homocitrate on this three electron-reduced species has been proposed to free up a binding site for N2 on the molybdenum atom. One of the features of this hypothesis is that α-Lys426 facilitates chelate ring opening and subsequent orientation of the monodentate homocitrate by forming a specific hydrogen bond to the homocitrate -CH2CH2CO2− carboxylate group. In support of this concept, we show that mutation of α-Lys426 can selectively perturb N2 reduction without affecting acetylene reduction. We interpret our experimental observations in the light of a detailed molecular mechanics modelling study of the wild-type and altered MoFe-nitrogenases.

Coordination of a Water Molecule to a Square-pyramidal N2S3-type Co(III) Complex Directed to an Active Site of Nitrile Hydratase

2005 ◽  
Vol 34 (1) ◽  
pp. 18-19 ◽  
Author(s):  
Tomohiro Ozawa ◽  
Tomohiro Ikeda ◽  
Takuma Yano ◽  
Hidekazu Arii ◽  
Syuhei Yamaguchi ◽  
...  
Keyword(s):  
Water Molecule ◽  
Active Site ◽  
Nitrile Hydratase
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